dc.contributor.author | Dobrovolska, Olena | |
dc.contributor.author | Shumilina, Elena | |
dc.contributor.author | Gladyshev, Vadim N. | |
dc.contributor.author | Dikiy, Alexander | |
dc.date.accessioned | 2015-10-30T14:15:34Z | |
dc.date.accessioned | 2015-11-24T14:55:00Z | |
dc.date.available | 2015-10-30T14:15:34Z | |
dc.date.available | 2015-11-24T14:55:00Z | |
dc.date.issued | 2012 | |
dc.identifier.citation | PLoS ONE 2012, 7(12) | nb_NO |
dc.identifier.issn | 1932-6203 | |
dc.identifier.uri | http://hdl.handle.net/11250/2365569 | |
dc.description.abstract | Thioredoxin glutathione reductase (TGR) is a member of the mammalian thioredoxin reductase family that has a monothiol
glutaredoxin (Grx) domain attached to the thioredoxin reductase module. Here, we report a structure of the Grx domain of
mouse TGR, determined through high resolution NMR spectroscopy to the final backbone RMSD value of 0.4860.10 A°
. The
structure represents a sandwich-like molecule composed of a four stranded b-sheet flanked by five a–helixes, with the CxxS
active motif located on the catalytic loop. We structurally characterized the glutathione-binding site in the protein and
describe sequence and structural relationships of the domain with glutaredoxins. The structure illuminates a key functional
center that evolved in mammalian TGRs to act in thiol-disulfide reactions. Our study allows us to hypothesize that Cys105
might be functionally relevant for TGR catalysis. In addition, the data suggest that the N-terminus of Grx acts as a possible
regulatory signal also protecting the protein active site from unwanted interactions in cellular cytosol. | nb_NO |
dc.language.iso | eng | nb_NO |
dc.publisher | Public Library of Science | nb_NO |
dc.title | Structural Analysis of Glutaredoxin Domain of Mus musculus Thioredoxin Glutathione Reductase | nb_NO |
dc.type | Journal article | nb_NO |
dc.type | Peer reviewed | en_GB |
dc.date.updated | 2015-10-30T14:15:34Z | |
dc.source.volume | 7 | nb_NO |
dc.source.journal | PLoS ONE | nb_NO |
dc.source.issue | 12 | nb_NO |
dc.identifier.doi | 10.1371/journal.pone.0052914 | |
dc.identifier.cristin | 982336 | |
dc.description.localcode | © 2012 Dobrovolska et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. | nb_NO |